| IED ID | IndEnz0002007823 |
| Enzyme Type ID | protease007823 |
| Protein Name |
Prolyl endopeptidase PE EC 3.4.21.26 Post-proline cleaving enzyme |
| Gene Name | PREP |
| Organism | Sus scrofa (Pig) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Suina Suidae (pigs) Sus Sus scrofa (Pig) |
| Enzyme Sequence | MLSFQYPDVYRDETAIQDYHGHKVCDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNILSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFSCMAWTHDGKGMFYNAYPQQDGKSDGTETSTNLHQKLYYHVLGTDQSEDILCAEFPDEPKWMGGAELSDDGRYVLLSIREGCDPVNRLWYCDLQQESNGITGILKWVKLIDNFEGEYDYVTNEGTVFTFKTNRHSPNYRLINIDFTDPEESKWKVLVPEHEKDVLEWVACVRSNFLVLCYLHDVKNTLQLHDLATGALLKIFPLEVGSVVGYSGQKKDTEIFYQFTSFLSPGIIYHCDLTKEELEPRVFREVTVKGIDASDYQTVQIFYPSKDGTKIPMFIVHKKGIKLDGSHPAFLYGYGGFNISITPNYSVSRLIFVRHMGGVLAVANIRGGGEYGETWHKGGILANKQNCFDDFQCAAEYLIKEGYTSPKRLTINGGSNGGLLVATCANQRPDLFGCVIAQVGVMDMLKFHKYTIGHAWTTDYGCSDSKQHFEWLIKYSPLHNVKLPEADDIQYPSMLLLTADHDDRVVPLHSLKFIATLQYIVGRSRKQNNPLLIHVDTKAGHGAGKPTAKVIEEVSDMFAFIARCLNIDWIP |
| Enzyme Length | 710 |
| Uniprot Accession Number | P23687 |
| Absorption | |
| Active Site | ACT_SITE 554; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:1900195"; ACT_SITE 641; /note="Charge relay system"; ACT_SITE 680; /note="Charge relay system"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10084, ECO:0000269|PubMed:2064618" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; |
| DNA Binding | |
| EC Number | 3.4.21.26 |
| Enzyme Function | FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (51); Chain (1); Helix (22); Modified residue (2); Natural variant (1); Turn (5) |
| Keywords | 3D-structure;Acetylation;Cytoplasm;Direct protein sequencing;Hydrolase;Protease;Reference proteome;Serine protease |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:P48147; MOD_RES 157; /note=N6-acetyllysine; /evidence=ECO:0000250|UniProtKB:P48147 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (28) |
| Cross Reference PDB | 1E5T; 1E8M; 1E8N; 1H2W; 1H2X; 1H2Y; 1H2Z; 1O6F; 1O6G; 1QFM; 1QFS; 1UOO; 1UOP; 1UOQ; 1VZ2; 1VZ3; 2XDW; 3EQ7; 3EQ8; 3EQ9; 4AMY; 4AMZ; 4AN0; 4AN1; 4AX4; 4BCB; 4BCC; 4BCD; |
| Mapped Pubmed ID | 11031266; 11256612; 12202494; 12228249; 14514675; 15210359; 19006380; 20627594; 22484394; 22940581; 23121075; |
| Motif | |
| Gene Encoded By | |
| Mass | 80,770 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.26; |